Filtros : "CRISTALOGRAFIA FÍSICA" "BIOQUÍMICA" Removido: "Resumos" Limpar

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  • Source: Journal of Biological Chemistry. Unidade: IF

    Subjects: BIOQUÍMICA, DIFRAÇÃO POR RAIOS X, CRISTALOGRAFIA FÍSICA

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    • ABNT

      BORGES, Julio Cesar et al. Low resolution structural study of two human HSP40 chaperonesin solution. Journal of Biological Chemistry, v. 280, p. 13671-13681, 2005Tradução . . Disponível em: http://intl.jbc.org/pips/pips.0.shtml. Acesso em: 27 nov. 2025.
    • APA

      Borges, J. C., Fischer, H., Craievich, A. F., & Ramos, C. H. I. (2005). Low resolution structural study of two human HSP40 chaperonesin solution. Journal of Biological Chemistry, 280, 13671-13681. Recuperado de http://intl.jbc.org/pips/pips.0.shtml
    • NLM

      Borges JC, Fischer H, Craievich AF, Ramos CHI. Low resolution structural study of two human HSP40 chaperonesin solution [Internet]. Journal of Biological Chemistry. 2005 ; 280 13671-13681.[citado 2025 nov. 27 ] Available from: http://intl.jbc.org/pips/pips.0.shtml
    • Vancouver

      Borges JC, Fischer H, Craievich AF, Ramos CHI. Low resolution structural study of two human HSP40 chaperonesin solution [Internet]. Journal of Biological Chemistry. 2005 ; 280 13671-13681.[citado 2025 nov. 27 ] Available from: http://intl.jbc.org/pips/pips.0.shtml
  • Source: Protein Science. Unidades: IF, IFSC

    Subjects: CRISTALOGRAFIA FÍSICA, BIOQUÍMICA, BIOLOGIA MOLECULAR

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    • ABNT

      FISCHER, Hannes e POLIKARPOV, Igor e CRAIEVICH, Aldo Felix. Average protein density is a molecular-weight-dependent function. Protein Science, 2004Tradução . . Disponível em: https://doi.org/10.1110/ps.04688204. Acesso em: 27 nov. 2025.
    • APA

      Fischer, H., Polikarpov, I., & Craievich, A. F. (2004). Average protein density is a molecular-weight-dependent function. Protein Science. doi:10.1110/ps.04688204
    • NLM

      Fischer H, Polikarpov I, Craievich AF. Average protein density is a molecular-weight-dependent function [Internet]. Protein Science. 2004 ;[citado 2025 nov. 27 ] Available from: https://doi.org/10.1110/ps.04688204
    • Vancouver

      Fischer H, Polikarpov I, Craievich AF. Average protein density is a molecular-weight-dependent function [Internet]. Protein Science. 2004 ;[citado 2025 nov. 27 ] Available from: https://doi.org/10.1110/ps.04688204
  • Source: Journal of Biological Chemistry. Unidades: IF, IFSC

    Subjects: BIOLOGIA MOLECULAR, CRISTALOGRAFIA FÍSICA, DNA, BIOQUÍMICA, PROTEÍNAS

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    • ABNT

      FISCHER, Hannes et al. Low resolution structures of the retinoid X receptor DNA-binding and ligand-binding domains revealed by synchrotron X-ray solution scattering. Journal of Biological Chemistry, v. 278, n. 18, p. 16030-16038, 2003Tradução . . Acesso em: 27 nov. 2025.
    • APA

      Fischer, H., Dias, S. M. G., Santos, M. A. M., Alves, A. C., Zanchin, N., Craievich, A. F., et al. (2003). Low resolution structures of the retinoid X receptor DNA-binding and ligand-binding domains revealed by synchrotron X-ray solution scattering. Journal of Biological Chemistry, 278( 18), 16030-16038.
    • NLM

      Fischer H, Dias SMG, Santos MAM, Alves AC, Zanchin N, Craievich AF, Apriletti JW, Baxter J, Webb P, Neves FAR, Ribeiro RCJ, Polikarpov I. Low resolution structures of the retinoid X receptor DNA-binding and ligand-binding domains revealed by synchrotron X-ray solution scattering. Journal of Biological Chemistry. 2003 ; 278( 18): 16030-16038.[citado 2025 nov. 27 ]
    • Vancouver

      Fischer H, Dias SMG, Santos MAM, Alves AC, Zanchin N, Craievich AF, Apriletti JW, Baxter J, Webb P, Neves FAR, Ribeiro RCJ, Polikarpov I. Low resolution structures of the retinoid X receptor DNA-binding and ligand-binding domains revealed by synchrotron X-ray solution scattering. Journal of Biological Chemistry. 2003 ; 278( 18): 16030-16038.[citado 2025 nov. 27 ]
  • Source: Biochemistry. Unidade: IF

    Subjects: CRISTALOGRAFIA FÍSICA, DIFRAÇÃO POR RAIOS X, BIOQUÍMICA

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    • ABNT

      APARICIO, Ricardo et al. Structural insights into the 'beta'-mannosidase from T. reesei obtained by synchrotron small-angle X-ray solution scattering enhanced by X-ray crystallography. Biochemistry, v. 41, n. 30, p. 9370-9375, 2002Tradução . . Disponível em: http://pubs.acs.org/journals/bichaw/article.cgi/bichaw/2002/41/i30/pdf/bi025811p.pdf. Acesso em: 27 nov. 2025.
    • APA

      Aparicio, R., Fischer, H., Scott, D. J., Verschueren, K. H. G., Kulminskaya, A. A., Eneiskaya, E. V., et al. (2002). Structural insights into the 'beta'-mannosidase from T. reesei obtained by synchrotron small-angle X-ray solution scattering enhanced by X-ray crystallography. Biochemistry, 41( 30), 9370-9375. Recuperado de http://pubs.acs.org/journals/bichaw/article.cgi/bichaw/2002/41/i30/pdf/bi025811p.pdf
    • NLM

      Aparicio R, Fischer H, Scott DJ, Verschueren KHG, Kulminskaya AA, Eneiskaya EV, Neustroev KN, Craievich AF, Golubev AM, Polikarpov I. Structural insights into the 'beta'-mannosidase from T. reesei obtained by synchrotron small-angle X-ray solution scattering enhanced by X-ray crystallography [Internet]. Biochemistry. 2002 ; 41( 30): 9370-9375.[citado 2025 nov. 27 ] Available from: http://pubs.acs.org/journals/bichaw/article.cgi/bichaw/2002/41/i30/pdf/bi025811p.pdf
    • Vancouver

      Aparicio R, Fischer H, Scott DJ, Verschueren KHG, Kulminskaya AA, Eneiskaya EV, Neustroev KN, Craievich AF, Golubev AM, Polikarpov I. Structural insights into the 'beta'-mannosidase from T. reesei obtained by synchrotron small-angle X-ray solution scattering enhanced by X-ray crystallography [Internet]. Biochemistry. 2002 ; 41( 30): 9370-9375.[citado 2025 nov. 27 ] Available from: http://pubs.acs.org/journals/bichaw/article.cgi/bichaw/2002/41/i30/pdf/bi025811p.pdf

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